GUDIS_FUSMA
ID GUDIS_FUSMA Reviewed; 401 AA.
AC A0A1L7U8F2;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 1.
DT 03-AUG-2022, entry version 13.
DE RecName: Full=(1R,4R,5S)-(-)-guaia-6,10(14)-diene synthase {ECO:0000303|PubMed:27294564};
DE EC=4.2.3.165 {ECO:0000269|PubMed:27294564};
DE AltName: Full=Sesquiterpene cyclase {ECO:0000303|PubMed:27294564};
DE AltName: Full=Terpene synthase {ECO:0000303|PubMed:27294564};
DE AltName: Full=Type I terpene cyclase {ECO:0000303|PubMed:27294564};
GN ORFNames=FMAN_14887 {ECO:0000312|EMBL:CVL03997.1};
OS Fusarium mangiferae (Mango malformation disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=192010;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRC7560;
RX PubMed=28040774; DOI=10.1093/gbe/evw259;
RA Niehaus E.-M., Muensterkoetter M., Proctor R.H., Brown D.W., Sharon A.,
RA Idan Y., Oren-Young L., Sieber C.M., Novak O., Pencik A., Tarkowska D.,
RA Hromadova K., Freeman S., Maymon M., Elazar M., Youssef S.A.,
RA El-Shabrawy E.S.M., Shalaby A.B.A., Houterman P., Brock N.L., Burkhardt I.,
RA Tsavkelova E.A., Dickschat J.S., Galuszka P., Gueldener U., Tudzynski B.;
RT "Comparative 'omics' of the Fusarium fujikuroi species complex highlights
RT differences in genetic potential and metabolite synthesis.";
RL Genome Biol. Evol. 8:3574-3599(2016).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, DOMAIN, AND REACTION
RP MECHANISM.
RX PubMed=27294564; DOI=10.1002/anie.201603782;
RA Burkhardt I., Siemon T., Henrot M., Studt L., Roesler S., Tudzynski B.,
RA Christmann M., Dickschat J.S.;
RT "Mechanistic characterisation of two sesquiterpene cyclases from the plant
RT pathogenic fungus Fusarium fujikuroi.";
RL Angew. Chem. Int. Ed. 55:8748-8751(2016).
CC -!- FUNCTION: Catalyzes the conversion of (2E,6E)-farnesyl diphosphate
CC (FPP) to yield the bicyclic sesquiterpene guaia-6,10(14)-diene via a
CC 1,10-cyclization, which requires the abstraction of the pyrophosphate
CC from FPP to yield the (E,E)-germacradienyl cation. The only accepted
CC substrate is farnesyl diphosphate (FPP). {ECO:0000269|PubMed:27294564}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (1R,4R,5S)-(-)-guaia-6,10(14)-
CC diene + diphosphate; Xref=Rhea:RHEA:53668, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:137563, ChEBI:CHEBI:175763; EC=4.2.3.165;
CC Evidence={ECO:0000269|PubMed:27294564};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:B5HDJ6};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:B5HDJ6};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305}.
CC -!- DOMAIN: The Asp-Asp-Xaa-Xaa-Asp (DDXXD) motif is important for the
CC catalytic activity, presumably through binding to Mg(2+).
CC {ECO:0000305|PubMed:27294564}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; FCQH01000014; CVL03997.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L7U8F2; -.
DR SMR; A0A1L7U8F2; -.
DR OrthoDB; 1143139at2759; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000184255; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.600.10; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR034686; Terpene_cyclase-like_2.
DR SFLD; SFLDG01020; Terpene_Cyclase_Like_2; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Lyase; Magnesium; Metal-binding.
FT CHAIN 1..401
FT /note="(1R,4R,5S)-(-)-guaia-6,10(14)-diene synthase"
FT /id="PRO_0000443320"
FT MOTIF 134..138
FT /note="DDXXD motif"
FT /evidence="ECO:0000305|PubMed:27294564"
FT BINDING 134
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 139
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 139
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 242
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 288
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 292
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 295
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 296
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 375..376
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
SQ SEQUENCE 401 AA; 45843 MW; 59740D71C76183A6 CRC64;
MVKFDSGSES EMTNGDEVHI NTKHEVKSRM ANGNGVHNVP DHDQFQDRAE MEVLILPDLF
SSLMSVPARE NPHYASVKAD ADEWISSVIN ADAKWASRNK RVDFTYLASI WAPDCSAFAL
RTSADWNSWA FLFDDQFDEG HLSNDLDGAI NEIARTREIM EGTAPRYTAD SEHPIRYVFQ
TLCDRVKQSP EGFYAGKPSS DRFYRRWMWA HELYWEGLVA QVRTNVEGRS FTRGPEEYLA
MRRGSLGAYP ALVNNEWAYG IDLPEDVADH PLVFEIMVIM SDQILLVNDI LSYEKDLRLG
VDHNMVRLLK AKGLSTQQAI NEVGVMINNC YRRYYRALSE LPCFGEEADR ALLGYLEVEK
NHALGSLLWS YKTGRYFKSK EDGARVRKTR ELLIPKKMAA L
